ID A0A135TGK6_9PEZI Unreviewed; 1111 AA.
AC A0A135TGK6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=valine--tRNA ligase {ECO:0000256|ARBA:ARBA00013169};
DE EC=6.1.1.9 {ECO:0000256|ARBA:ARBA00013169};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029936};
GN ORFNames=CSAL01_08463 {ECO:0000313|EMBL:KXH47306.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH47306.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH47306.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH47306.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00001624};
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|RuleBase:RU363035}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXH47306.1}.
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DR EMBL; JFFI01001982; KXH47306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135TGK6; -.
DR STRING; 1209931.A0A135TGK6; -.
DR OrthoDB; 5473263at2759; -.
DR Proteomes; UP000070121; Unassembled WGS sequence.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR CDD; cd00817; ValRS_core; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR NCBIfam; TIGR00422; valS; 1.
DR PANTHER; PTHR11946:SF109; VALINE--TRNA LIGASE; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|RuleBase:RU363035};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU363035};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU363035};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU363035};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU363035};
KW Reference proteome {ECO:0000313|Proteomes:UP000070121}.
FT DOMAIN 145..767
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 810..946
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1039..1108
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 25..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1111 AA; 124331 MW; A693C508A4D854A3 CRC64;
MATDSGRGNP IGATEGLKEQ APPAVSNETK AQVASTDATH AAGQDAGATT GAPPKVKTEK
ELEKERKKAE KDAKFKAKLA EKAAKAAAAP AASKNKEKKA KAEKKEEEAI PEYVEDTPKG
EKKRLKPLED PHFKAYHPEA VESAWYDWWE QEGFFKPEFT ADGKVKPAGK FVIAHPPPNV
TGALHLGHAL GDSLQDIMIR WNRMLGKTTL WIPGCDHAGI STQSVVENML WRREGKTRHD
LGREDFVDKV WTWKGEYHDK INAALRKMGG SFDWSREAFT MDANLSAAVA ETFVRLFEEG
TIYRANRLVN WSSRLTTALS NLEVINKELT GRTLLEVPGY EKKIEFGVLI HFKYQIEGTD
EYLEVATTRI ETMLGDSGIA VHPDDPRYTH LVGKKAVHPI IEGRLMPIVA DTYVDKEFGT
GAVKLTPAHD PNDFNLGQKH GLEFINILTD DGNINENGGK YQGQKRFDVR YAIQEELKQL
GLYVDKKDNA MTIPLCERSK DVIEPLLKPQ WYMSMRSMAD DAVAAVKDGR IKIKPESSER
SFYAWMANIN DWCISRQLWW GHRCPVYLAK VEGEKSDSLD NKRWFAGKNR EEAEAKAKAA
LPGKTFTLEQ DEDVLDTWFS SGLWPFSTLG WPNKTQDLQE LYPTSVLETG WDILFFWIAR
MVMLGIKLTG QVPFTEVYCH SLVRDSEGRK MSKSLGNVID PLDAIAGIKL EDLHAKLRTG
NLHPSEVAKA EKYQKVAFPD GLPRNGADSL RFTMAALTST SGDVNFDVKV MTGWRKFCNK
IWQASKYVLG NLPADFVPAK EATVGVTLAE KWILHKLNNA AKEINTALAA RDFQQATGIV
YQYILNFLCD VYIENSKSII RDGTPEEAAS AVQTLYTVLE GALTMIHPFT PFLTEELWQR
LPRRPEDKTR SIMLASYPVY DAKFDDPKSE AAYELVLGCS RGARSLMSEY AQKEESKSKP
PVSMLRCRSR PLTRTEVIIQ SHDATSHQTI NDQVASIKTL SGKGVTGIDI IASDAARPAG
CVAFPVASSA SVYLHVKGRV DLDAEVEKAK KRLDKARANI DKQHKVLNDP IYKEKVAEAV
QKLDKQKLVD LESEARSFED TIKQFEQLKL E
//
